Principles of protein-protein association / Harold P. Erickson.

By: Erickson, Harold P [author.]Contributor(s): Institute of Physics (Great Britain) [publisher.]Material type: TextTextSeries: IOP (Series)Release 6 | IOP expanding physics | Biophysical Society seriesPublisher: Bristol [England] (Temple Circus, Temple Way, Bristol BS1 6HG, UK) : IOP Publishing, [2019]Description: 1 online resource (various pagings) : illustrations (some color)Content type: text Media type: electronic Carrier type: online resourceISBN: 9780750324120 ebookSubject(s): Protein-protein interactions | Proteins -- physiology | Protein Interaction Mapping | Biophysics | SCIENCE / Life Sciences / BiophysicsAdditional physical formats: Print version:: No titleDDC classification: 572/.64 LOC classification: QP551.5 .E757 2019ebNLM classification: QU 55Online resources: e-book Full-text access Also available in print.
Contents:
1. Size and shape of protein molecules at the nm level determined by sedimentation, gel filtration and electron microscopy -- 1.1. Introduction -- 1.2. How big is a protein molecule? -- 1.3. How far apart are molecules in solution? -- 1.4. The s
2. Basic thermodynamics of reversible association -- 3. The nature of the protein-protein bond, �a la Chothia and Janin -- 3.1. Hydrogen bonds and ionic bonds in proteins -- 3.2. The simplified protein bond model of Chothia and Janin -- 3.
4. The structure of an antibody bound to its protein ligand--lock and key versus induced fit and conformational selection -- 4.1. Nature's site-directed mutagenesis experiment -- 4.2. Induced fit and conformational selection
5. The complex of growth hormone with its receptor--one protein interface binds two partners -- 5.1. GHR binds two different patches on opposite sides of GH -- 5.2. Other proteins with multiple binding partners
6. The hot spot in protein-protein interfaces -- 6.1. Hot spot paper one--the technology and alanine scanning of GH -- 6.2. Hot spot paper two--scanning GHR and matching the hot spots -- 6.3. Plasticity in the evolution of protein-protein interf
7. Cooperativity in protein-protein association and efficiency of bonds -- 7.1. Intrinsic bond energy and subunit entropy -- 7.2. Additivity of bond energies and cooperative association -- 7.3. Analysis of cooperativity in GH-GHR association, an
8. Kinetics of protein-protein association and dissociation -- 8.1. What is the half time of the empty receptor? -- 8.2. What is the half time of the complex? -- 8.3. The diffusion-limited rate constant for protein-protein association -- 8.4. Ha
9. Techniques for measuring protein-protein association--use and misuse of ELISA -- 9.1. Qualitative assays to screen for protein-protein association in vivo -- 9.2. Quantitative methods for measuring the KD of protein-protein association -- 9.3
10. Fibronectin, the FNIII domain, and artificial antibodies -- 10.1. Fibronectin, cell adhesion and RGD -- 10.2. Antibody mimics--creating novel binding activities in a neutral protein framework -- 11. Association of intrinsically disordered pr
Abstract: Protein-protein associations are fundamental to biological mechanisms, creating a need for a book that covers the basic principles of protein-protein association. This book has been developed from lectures given to graduate students in cell and
Item type Current library Collection Call number Copy number Status Date due Barcode
E-Books MEF eKitap Kütüphanesi
IOP Science eBook - EBA QP551.5 .E757 2019eb (Browse shelf (Opens below)) Available IOP_20210123

"Version: 20190601"--Title page verso.

Includes bibliographical references.

1. Size and shape of protein molecules at the nm level determined by sedimentation, gel filtration and electron microscopy -- 1.1. Introduction -- 1.2. How big is a protein molecule? -- 1.3. How far apart are molecules in solution? -- 1.4. The s

2. Basic thermodynamics of reversible association -- 3. The nature of the protein-protein bond, �a la Chothia and Janin -- 3.1. Hydrogen bonds and ionic bonds in proteins -- 3.2. The simplified protein bond model of Chothia and Janin -- 3.

4. The structure of an antibody bound to its protein ligand--lock and key versus induced fit and conformational selection -- 4.1. Nature's site-directed mutagenesis experiment -- 4.2. Induced fit and conformational selection

5. The complex of growth hormone with its receptor--one protein interface binds two partners -- 5.1. GHR binds two different patches on opposite sides of GH -- 5.2. Other proteins with multiple binding partners

6. The hot spot in protein-protein interfaces -- 6.1. Hot spot paper one--the technology and alanine scanning of GH -- 6.2. Hot spot paper two--scanning GHR and matching the hot spots -- 6.3. Plasticity in the evolution of protein-protein interf

7. Cooperativity in protein-protein association and efficiency of bonds -- 7.1. Intrinsic bond energy and subunit entropy -- 7.2. Additivity of bond energies and cooperative association -- 7.3. Analysis of cooperativity in GH-GHR association, an

8. Kinetics of protein-protein association and dissociation -- 8.1. What is the half time of the empty receptor? -- 8.2. What is the half time of the complex? -- 8.3. The diffusion-limited rate constant for protein-protein association -- 8.4. Ha

9. Techniques for measuring protein-protein association--use and misuse of ELISA -- 9.1. Qualitative assays to screen for protein-protein association in vivo -- 9.2. Quantitative methods for measuring the KD of protein-protein association -- 9.3

10. Fibronectin, the FNIII domain, and artificial antibodies -- 10.1. Fibronectin, cell adhesion and RGD -- 10.2. Antibody mimics--creating novel binding activities in a neutral protein framework -- 11. Association of intrinsically disordered pr

Protein-protein associations are fundamental to biological mechanisms, creating a need for a book that covers the basic principles of protein-protein association. This book has been developed from lectures given to graduate students in cell and

Graduate students in biochemistry and cell biology.

Also available in print.

Mode of access: World Wide Web.

System requirements: Adobe Acrobat Reader, EPUB reader, or Kindle reader.

Dr. Erickson is a Professor in the Departments of Cell Biology, Biochemistry and Biomedical Engineering at Duke University. Having received his PhD in biophysics from Johns Hopkins University in 1968, he did postdoctoral work with Aaron Klug at

Title from PDF title page (viewed on July 2, 2019).